The DOI matches its Crossref record.
Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy
Open accessAbstract
Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One‐ and two‐dimensional solid‐state 15 N NMR spectra of specifically 15 N‐labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is α‐helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.
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Citations
Cited by
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Self-citationAntimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Bayer, A. S., Prasad, R., Chandra, J., Koul, A., Smriti, M., Varma, A., Skurray, R. A., Firth, N., Brown, M. H., Koo, S.-P., et al. (2000) · Infection and Immunity · doi:10.1128/iai.68.6.3548-3553.2000 · Cited by 150
Metadata
- Authors
- Bechinger, B., Zasloff, M., & Opella, S. J.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 1993-12
- Volume
- 2
- Issue
- 12
- Pages
- 2077-2084
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2148662470
- Cited by
- 357
- References
- 0
- FWCI
- 6.44
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
